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3 results on '"INRA AlimH department"'

1. Gene Expression Profiling Reveals that PXR Activation Inhibits Hepatic PPARα Activity and Decreases FGF21 Secretion in Male C57Bl6/J Mice

Author

Tiffany Fougeray, Marion Régnier, Nicolas Loiseau, Colette Bétoulières, Yannick Lippi, Arnaud Polizzi, Hervé Guillou, Laila Mselli-Lakhal, Céline Lukowicz, Frédéric Lasserre, Claire Naylies, Anne Fougerat, Sharon Barretto, Laurence Gamet-Payrastre, Sarra Smati, Sandrine Ellero-Simatos, Lorraine Smith, ToxAlim (ToxAlim), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Ecole Nationale Vétérinaire de Toulouse (ENVT), Institut National Polytechnique (Toulouse) (Toulouse INP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Ecole d'Ingénieurs de Purpan (INPT - EI Purpan), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Recherche Agronomique (INRA), Toxicologie Intégrative & Métabolisme (ToxAlim-TIM), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Recherche Agronomique (INRA)-Université Toulouse III - Paul Sabatier (UT3), Transcriptomic impact of Xenobiotics (E23 TRiX), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Recherche Agronomique (INRA)-Plateforme Génome & Transcriptome (GET), Génopole Toulouse Midi-Pyrénées [Auzeville] (GENOTOUL), Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Ecole Nationale Vétérinaire de Toulouse (ENVT), Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Génopole Toulouse Midi-Pyrénées [Auzeville] (GENOTOUL), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Plateforme Ezop (Ezop), Exposition, Perturbation Endocrino-métabolique et Reproduction (ToxAlim-EXPER), Region Occitanie, INRA AlimH department, Agence Nationale de la Recherche (ANR), Fond Europeen de Developpement Regional (FEDER), Joint Programming Initiative (JPI), Institut National de la Recherche Agronomique (INRA)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Ecole d'Ingénieurs de Purpan (INPT - EI Purpan), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Plateforme Génome & Transcriptome (GET), Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), and ElleroSsimatos, Sandrine

Subjects
Male, FGF21, nuclear receptors, Energy homeostasis, Transcriptome, lcsh:Chemistry, transcriptomics, 0302 clinical medicine, Receptor, lcsh:QH301-705.5, Spectroscopy, 0303 health sciences, Pregnane X receptor, hepatokines, Chemistry, Pregnane X Receptor, General Medicine, 3. Good health, Computer Science Applications, Cell biology, Liver, Pregnenolone, medicine.drug, Transcriptional Activation, digestive system, Catalysis, Article, Inorganic Chemistry, 03 medical and health sciences, Autre (Chimie), medicine, Animals, PPAR alpha, Physical and Theoretical Chemistry, Molecular Biology, 030304 developmental biology, Gene Expression Profiling, Organic Chemistry, digestive system diseases, Gene expression profiling, Fibroblast Growth Factors, Mice, Inbred C57BL, Nuclear receptor, lcsh:Biology (General), lcsh:QD1-999, Other, [CHIM.OTHE]Chemical Sciences/Other, 030217 neurology & neurosurgery, Gene Deletion
Abstract

The pregnane X receptor (PXR) is the main nuclear receptor regulating the expression of xenobiotic-metabolizing enzymes and is highly expressed in the liver and intestine. Recent studies have highlighted its additional role in lipid homeostasis, however, the mechanisms of these regulations are not fully elucidated. We investigated the transcriptomic signature of PXR activation in the liver of adult wild-type vs. Pxr-/- C57Bl6/J male mice treated with the rodent specific ligand pregnenolone 16&alpha, carbonitrile (PCN). PXR activation increased liver triglyceride accumulation and significantly regulated the expression of 1215 genes, mostly xenobiotic-metabolizing enzymes. Among the down-regulated genes, we identified a strong peroxisome proliferator-activated receptor &alpha, (PPAR&alpha, ) signature. Comparison of this signature with a list of fasting-induced PPAR&alpha, target genes confirmed that PXR activation decreased the expression of more than 25 PPAR&alpha, target genes, among which was the hepatokine fibroblast growth factor 21 (Fgf21). PXR activation abolished plasmatic levels of FGF21. We provide a comprehensive signature of PXR activation in the liver and identify new PXR target genes that might be involved in the steatogenic effect of PXR. Moreover, we show that PXR activation down-regulates hepatic PPAR&alpha, activity and FGF21 circulation, which could participate in the pleiotropic role of PXR in energy homeostasis.

Published
2019
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2. Biosynthesis of F-0, Precursor of the F-420 Cofactor, Requires a Unique Two Radical-SAM Domain Enzyme and Tyrosine as Substrate

Author

Benjamin Philmus, Robert H. White, Laure Decamps, Alhosna Benjdia, Olivier Berteau, Tadhg P. Begley, MICrobiologie de l'ALImentation au Service de la Santé (MICALIS), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Dept Chem, Texas A&M University [College Station], Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research [Heidelberg], Max-Planck-Gesellschaft-Max-Planck-Gesellschaft, Dept Biochem, Virginia Polytechnic Institute and State University [Blacksburg], INRA, AlimH department, Robert A. Welch Foundation [A-0034], and National Science Foundation [MCB0722787]

Subjects
[SDV.SA]Life Sciences [q-bio]/Agricultural sciences, S-Adenosylmethionine, Methanococcus, SULFATASE-MATURATING ENZYMES, 010402 general chemistry, COENZYME F-420, 01 natural sciences, Biochemistry, RIBOFLAVIN, Catalysis, Cofactor, NO, Riboflavin Synthase, 03 medical and health sciences, chemistry.chemical_compound, Colloid and Surface Chemistry, Biosynthesis, 8-DIDEMETHYL-8-HYDROXY-5-DEAZARIBOFLAVIN, Actinomycetales, Tyrosine, Nostoc, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, biology, IDENTIFICATION, Substrate (chemistry), General Chemistry, SUPERFAMILY, biology.organism_classification, Protein Structure, Tertiary, 0104 chemical sciences, Metabolic pathway, Enzyme, chemistry, ESCHERICHIA-COLI, biology.protein, MYCOBACTERIUM-TUBERCULOSIS, Radical SAM, MOAA, Archaea
Abstract

Cofactors play key roles in metabolic pathways. Among them F(420) has proved to be a very attractive target for the selective inhibition of archaea and actinobacteria. Its biosynthesis, in a unique manner, involves a key enzyme, F(0)-synthase. This enzyme is a large monomer in actinobacteria, while it is constituted of two subunits in archaea and cyanobacteria. We report here the purification of both types of F(0)-synthase and their in vitro activities. Our study allows us to establish that F(0)-synthase, from both types, uses 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione and tyrosine as substrates but not 4-hydroxylphenylpyruvate as previously suggested. Furthermore, our data support the fact that F(0)-synthase generates two 5'-deoxyadenosyl radicals for catalysis which is unprecedented in reaction catalyzed by radical SAM enzymes.

Published
2012
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3. The ins and outs of cholesterol in the vertebrate retina

Author

Steven J. Fliesler, Lionel Bretillon, United States Department of Veterans Affairs, Partenaires INRAE, Departments of Ophthalmology and Biochemistry, Boston University School of Medicine (BUSM), Boston University [Boston] (BU)-Boston University [Boston] (BU), Centre des Sciences du Goût et de l'Alimentation (CSGA), Institut National de la Recherche Agronomique (INRA)-Université de Bourgogne (UB)-Centre National de la Recherche Scientifique (CNRS), United States Public Health Service (National Institutes of Health/National Eye Institute) [EY007361], March of Dimes Foundation, Research to Prevent Blindness, INRA AlimH Department, French Regional Council of Burgundy, and Fliesler, Steven J.

Subjects
QD415-436, Degeneration (medical), Biology, Blood–brain barrier, Biochemistry, Retina, 03 medical and health sciences, chemistry.chemical_compound, Smith-Lemli-Opitz syndrome, 0302 clinical medicine, Endocrinology, [SDV.IDA]Life Sciences [q-bio]/Food engineering, medicine, Animals, Humans, [SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering, cholesterol/biosynthesis, eye/retina, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, Cholesterol, Thematic Review, Biological Transport, Cell Biology, medicine.disease, Sterol, De novo synthesis, medicine.anatomical_structure, Enzyme, chemistry, Blood-Brain Barrier, Smith–Lemli–Opitz syndrome, Vertebrates, 030221 ophthalmology & optometry, lipids (amino acids, peptides, and proteins), sense organs
Abstract

Thematic Review Series: Lipids and Lipid Metabolism in the Eye; International audience; The vertebrate retina has multiple demands for utilization of cholesterol and must meet those demands either by synthesizing its own supply of cholesterol or by importing cholesterol from extraretinal sources, or both. Unlike the blood-brain barrier, the blood-retina barrier allows uptake of cholesterol from the circulation via a lipoprotein-based/receptor-mediated mechanism. Under normal conditions, cholesterol homeostasis is tightly regulated; also, cholesterol exists in the neural retina overwhelmingly in unesterified form, and sterol intermediates are present in minimal to negligible quantities. However, under certain pathological conditions, either due to an inborn error in cholesterol biosynthesis or as a consequence of exposure to selective inhibitors of enzymes in the cholesterol pathway, the ratio of sterol intermediates to cholesterol in the retina can rise dramatically and persist, in some cases resulting in progressive degeneration that significantly compromises the structure and function of the retina. Although the relative contributions of de novo synthesis versus extraretinal uptake are not yet known, herein we review what is known about these processes and the dynamics of cholesterol in the vertebrate retina and indicate some future avenues of research in this area.

Published
2010
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